Structure of PDB 6vtv Chain B Binding Site BS01

Receptor Information

>6vtv Chain B (length=252) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

NIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEP
SLLEQLLPKLDGIYLPGSPSNVQPHLYGENGDEPDADPGRDLLSMAIINA
ALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQ
YAPSHEVQVEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPD
GLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAEKQ
RL

Ligand information

Ligand ID

InChI

InChI=1S/Mn/q+2

InChIKey

WAEMQWOKJMHJLA-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mn+2]
CACTVS 3.341	[Mn++]

Formula

Name

MANGANESE (II) ION

PDB chain

6vtv Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	6vtv PuuD gamma-glutamyl-gamma-aminobutyrate hydrolase
Resolution	2.06 Å
Binding residue (original residue number in PDB)	H145 H161 S185 H187 E210
Binding residue (residue number reindexed from 1)	H139 H155 S179 H181 E204
Annotation score	1

Enzymatic activity

Enzyme Commision number

3.5.1.94: gamma-glutamyl-gamma-aminobutyrate hydrolase.

Gene Ontology

	Molecular Function
GO:0016787	hydrolase activity
GO:0016811	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0033969	gamma-glutamyl-gamma-aminobutyrate hydrolase activity

	Biological Process
GO:0006598	polyamine catabolic process
GO:0009447	putrescine catabolic process

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Molecular Function

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Biological Process

External links

PDB	RCSB:6vtv, PDBe:6vtv, PDBj:6vtv
PDBsum	6vtv
PubMed
UniProt	P76038\|PUUD_ECOLI Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (Gene Name=puuD)

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